1hm6
From Proteopedia
(New page: 200px<br /><applet load="1hm6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hm6, resolution 1.80Å" /> '''X-RAY STRUCTURE OF F...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1hm6.gif|left|200px]]<br /><applet load="1hm6" size=" | + | [[Image:1hm6.gif|left|200px]]<br /><applet load="1hm6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hm6, resolution 1.80Å" /> | caption="1hm6, resolution 1.80Å" /> | ||
'''X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1'''<br /> | '''X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Annexins comprise a multigene family of Ca2+ and phospholipid- binding | + | Annexins comprise a multigene family of Ca2+ and phospholipid- binding proteins. They consist of a conserved C-terminal or core domain that confers Ca2+-dependent phospholipid binding and an N-terminal domain that is variable in sequence and length and responsible for the specific properties of each annexin. Crystal structures of various annexin core domains have revealed a high degree of similarity. From these and other studies it is evident that the core domain harbors the calcium-binding sites that interact with the phospholipid headgroups. However, no structure has been reported of an annexin with a complete N-terminal domain. We have now solved the crystal structure of such a full-length annexin, annexin 1. Annexin 1 is active in membrane aggregation and its refined 1.8 A structure shows an alpha-helical N-terminal domain connected to the core domain by a flexible linker. It is surprising that the two alpha-helices present in the N-terminal domain of 41 residues interact intimately with the core domain, with the amphipathic helix 2-12 of the N-terminal domain replacing helix D of repeat III of the core. In turn, helix D is unwound into a flap now partially covering the N-terminal helix. Implications for membrane aggregation will be discussed and a model of aggregation based on the structure will be presented. |
==About this Structure== | ==About this Structure== | ||
| - | 1HM6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1HM6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HM6 OCA]. |
==Reference== | ==Reference== | ||
| Line 21: | Line 21: | ||
[[Category: phospholipid/ca(2+)-binding protein]] | [[Category: phospholipid/ca(2+)-binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:39 2008'' |
Revision as of 11:02, 21 February 2008
|
X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1
Overview
Annexins comprise a multigene family of Ca2+ and phospholipid- binding proteins. They consist of a conserved C-terminal or core domain that confers Ca2+-dependent phospholipid binding and an N-terminal domain that is variable in sequence and length and responsible for the specific properties of each annexin. Crystal structures of various annexin core domains have revealed a high degree of similarity. From these and other studies it is evident that the core domain harbors the calcium-binding sites that interact with the phospholipid headgroups. However, no structure has been reported of an annexin with a complete N-terminal domain. We have now solved the crystal structure of such a full-length annexin, annexin 1. Annexin 1 is active in membrane aggregation and its refined 1.8 A structure shows an alpha-helical N-terminal domain connected to the core domain by a flexible linker. It is surprising that the two alpha-helices present in the N-terminal domain of 41 residues interact intimately with the core domain, with the amphipathic helix 2-12 of the N-terminal domain replacing helix D of repeat III of the core. In turn, helix D is unwound into a flap now partially covering the N-terminal helix. Implications for membrane aggregation will be discussed and a model of aggregation based on the structure will be presented.
About this Structure
1HM6 is a Single protein structure of sequence from Sus scrofa with as ligand. Full crystallographic information is available from OCA.
Reference
X-ray structure of full-length annexin 1 and implications for membrane aggregation., Rosengarth A, Gerke V, Luecke H, J Mol Biol. 2001 Feb 23;306(3):489-98. PMID:11178908
Page seeded by OCA on Thu Feb 21 13:02:39 2008
